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Literature summary extracted from

  • Jahnova, J.; Luhova, L.; Petrivalsky, M.
    S-nitrosoglutathione reductase - the master regulator of protein S-nitrosation in plant NO signaling (2019), Plants (Basel), 8, 48 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.284 crystal structures of SlGSNOR apoenzyme, binary complex with NAD+ and a structure crystallized in the presence of NADH and GSH. Catalytic domains of the apoenzyme and of the binary complex with NAD+ are both in the semi-open conformation. The catalytic zinc atoms in the apoenzyme are in a tetrahedral configuration, H-bonded to Cys47, Cys177, His69 and coordinated to the molecule of water in the active site. The coenzyme binding is associated with the catalytic zinc atoms movement towards Glu70 in the catalytic domain in a hydrogen-bonding interaction with the carboxylate oxygen of Glu70. Zinc atoms are in a tetrahedral configuration coordinated with Cys47, Cys177, His69, and Glu70, and they are no longer coordinated with the water molecule. In the SlGSNOR structure crystallized with NADH and GSH, the enzyme appears in closed conformation. Structue analysis, overview Solanum lycopersicum

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.284 Cd2+ in pea leaves treated with 0.05 mM cadmium, GSNOR expression and activity are decreased by about 30% Pisum sativum
1.1.1.284 Decanoic acid noncompetitive inhibitor Solanum lycopersicum
1.1.1.284 dodecanoic acid noncompetitive inhibitor Solanum lycopersicum
1.1.1.284 GSH
-
Solanum lycopersicum
1.1.1.284 additional information GSNOR enzymatic activity, but not gene expression, is inhibited by the nitrogen assimilatory pathway via post-transcriptional S-nitrosation, preventing any scavenging of GSNO Arabidopsis thaliana
1.1.1.284 additional information lacking an S-nitrosyl or S-hydroxymethyl group that binds to the active site zinc atom, the affinity of inhibitors GSH and S-methylglutathione is reduced by 2-3 orders of magnitude compared to GSNO and HMGSH Solanum lycopersicum
1.1.1.284 N6022 a pyrolle-based compound, that is a significantly stronger noncompetitive inhibitor compared to fatty acids, inhibiting SlGSNOR at nanomolar concentrations Solanum lycopersicum
1.1.1.284 NO susceptibility of the enzymatic activity to NO donors in vitro and its subsequent restoration after treatment with reducing agent dithiothreitol (DTT) Arabidopsis thaliana
1.1.1.284 octanoic acid noncompetitive inhibitor Solanum lycopersicum
1.1.1.284 S-Methylglutathione
-
Solanum lycopersicum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.284 0.057
-
S-nitrosoglutathione pH and temperature not specified in the publication Solanum lycopersicum
1.1.1.284 0.058
-
S-(hydroxymethyl)glutathione pH and temperature not specified in the publication Solanum lycopersicum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.284 cytosol
-
Oryza sativa 5829
-
1.1.1.284 cytosol
-
Solanum lycopersicum 5829
-
1.1.1.284 cytosol
-
Arabidopsis thaliana 5829
-
1.1.1.284 cytosol
-
Nicotiana tabacum 5829
-
1.1.1.284 cytosol
-
Helianthus annuus 5829
-
1.1.1.284 cytosol
-
Cucumis sativus 5829
-
1.1.1.284 cytosol
-
Cucumis melo 5829
-
1.1.1.284 cytosol
-
Nicotiana attenuata 5829
-
1.1.1.284 cytosol
-
Solanum tuberosum 5829
-
1.1.1.284 cytosol
-
Pisum sativum 5829
-
1.1.1.284 cytosol
-
Lotus japonicus 5829
-
1.1.1.284 cytosol
-
Chlamydomonas reinhardtii 5829
-
1.1.1.284 mitochondrion the enzyme contains a mitochondrial targeting peptide Physcomitrium patens 5739
-
1.1.1.284 additional information modulation of the mitochondrial functionality by GSNOR, using cell suspension cultures with both higher and lower GSNOR levels, is demonstrated in Arabidopsis thaliana plants Arabidopsis thaliana
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.284 Zn2+ each catalytic domain includes two zinc atoms. One of them is involved in the catalytic mechanism by activating the hydroxyl and carbonyl groups of substrates for transfer of hydride, and is bonded to Cys47, Cys177, His69, and either Glu70 or a water molecule. The second zinc atom is considered to have purely a structural role and is coordinated to four cysteine residues, Cys99, Cys102, Cys105, and Cys113. From the crystal structure is determined, that the catalytic zinc atoms in the apoenzyme are in a tetrahedral configuration, H-bonded to Cys47, Cys177, His69 and coordinated to the molecule of water in the active site. The coenzyme binding is associated with the catalytic zinc atoms movement towards Glu70 in the catalytic domain in a hydrogen-bonding interaction with the carboxylate oxygen of Glu70. Zinc atoms are in a tetrahedral configuration coordinated with Cys47, Cys177, His69, and Glu70, and they are no longer coordinated with the water molecule Solanum lycopersicum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.284 additional information Oryza sativa in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO ?
-
-
1.1.1.284 additional information Solanum lycopersicum in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO ?
-
-
1.1.1.284 additional information Arabidopsis thaliana in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO ?
-
-
1.1.1.284 additional information Solanum tuberosum in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO ?
-
-
1.1.1.284 additional information Pisum sativum in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO ?
-
-
1.1.1.284 additional information Lotus japonicus in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO ?
-
-
1.1.1.284 additional information Chlamydomonas reinhardtii in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a cosubstrate in the reduction of GSNO ?
-
-
1.1.1.284 additional information Physcomitrium patens in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO ?
-
-
1.1.1.284 additional information Nicotiana tabacum in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO ?
-
-
1.1.1.284 additional information Helianthus annuus in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO ?
-
-
1.1.1.284 additional information Cucumis sativus in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO ?
-
-
1.1.1.284 additional information Cucumis melo in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO ?
-
-
1.1.1.284 additional information Nicotiana attenuata in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO ?
-
-
1.1.1.284 S-(hydroxymethyl)glutathione + NAD+ Oryza sativa
-
S-formylglutathione + NADH + H+
-
?
1.1.1.284 S-(hydroxymethyl)glutathione + NAD+ Solanum lycopersicum
-
S-formylglutathione + NADH + H+
-
?
1.1.1.284 S-(hydroxymethyl)glutathione + NAD+ Arabidopsis thaliana
-
S-formylglutathione + NADH + H+
-
?
1.1.1.284 S-(hydroxymethyl)glutathione + NAD+ Physcomitrium patens
-
S-formylglutathione + NADH + H+
-
?
1.1.1.284 S-(hydroxymethyl)glutathione + NAD+ Nicotiana tabacum
-
S-formylglutathione + NADH + H+
-
?
1.1.1.284 S-(hydroxymethyl)glutathione + NAD+ Helianthus annuus
-
S-formylglutathione + NADH + H+
-
?
1.1.1.284 S-(hydroxymethyl)glutathione + NAD+ Cucumis sativus
-
S-formylglutathione + NADH + H+
-
?
1.1.1.284 S-(hydroxymethyl)glutathione + NAD+ Cucumis melo
-
S-formylglutathione + NADH + H+
-
?
1.1.1.284 S-(hydroxymethyl)glutathione + NAD+ Nicotiana attenuata
-
S-formylglutathione + NADH + H+
-
?
1.1.1.284 S-(hydroxymethyl)glutathione + NAD+ Solanum tuberosum
-
S-formylglutathione + NADH + H+
-
?
1.1.1.284 S-(hydroxymethyl)glutathione + NAD+ Pisum sativum
-
S-formylglutathione + NADH + H+
-
?
1.1.1.284 S-(hydroxymethyl)glutathione + NAD+ Lotus japonicus
-
S-formylglutathione + NADH + H+
-
?
1.1.1.284 S-(hydroxymethyl)glutathione + NAD+ Chlamydomonas reinhardtii
-
S-formylglutathione + NADH + H+
-
?
1.1.1.284 S-nitrosoglutathione + NADH + H+ Oryza sativa
-
GSSG + ammonia + NAD+
-
ir
1.1.1.284 S-nitrosoglutathione + NADH + H+ Solanum lycopersicum
-
GSSG + ammonia + NAD+
-
ir
1.1.1.284 S-nitrosoglutathione + NADH + H+ Arabidopsis thaliana
-
GSSG + ammonia + NAD+
-
ir
1.1.1.284 S-nitrosoglutathione + NADH + H+ Physcomitrium patens
-
GSSG + ammonia + NAD+
-
ir
1.1.1.284 S-nitrosoglutathione + NADH + H+ Nicotiana tabacum
-
GSSG + ammonia + NAD+
-
ir
1.1.1.284 S-nitrosoglutathione + NADH + H+ Helianthus annuus
-
GSSG + ammonia + NAD+
-
ir
1.1.1.284 S-nitrosoglutathione + NADH + H+ Cucumis sativus
-
GSSG + ammonia + NAD+
-
ir
1.1.1.284 S-nitrosoglutathione + NADH + H+ Cucumis melo
-
GSSG + ammonia + NAD+
-
ir
1.1.1.284 S-nitrosoglutathione + NADH + H+ Nicotiana attenuata
-
GSSG + ammonia + NAD+
-
ir
1.1.1.284 S-nitrosoglutathione + NADH + H+ Solanum tuberosum
-
GSSG + ammonia + NAD+
-
ir
1.1.1.284 S-nitrosoglutathione + NADH + H+ Pisum sativum
-
GSSG + ammonia + NAD+
-
ir
1.1.1.284 S-nitrosoglutathione + NADH + H+ Lotus japonicus
-
GSSG + ammonia + NAD+
-
ir
1.1.1.284 S-nitrosoglutathione + NADH + H+ Chlamydomonas reinhardtii
-
GSSG + ammonia + NAD+
-
ir

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.284 Arabidopsis thaliana Q96533
-
-
1.1.1.284 Chlamydomonas reinhardtii A0A2K3D6Q9
-
-
1.1.1.284 Cucumis melo A0A1S3CB00
-
-
1.1.1.284 Cucumis sativus A0A0A0KBZ1
-
-
1.1.1.284 Helianthus annuus A0A251UXN7
-
-
1.1.1.284 Lotus japonicus I3ST14 Lotus corniculatus var. japonicus
-
1.1.1.284 Nicotiana attenuata A0A314KZZ1
-
-
1.1.1.284 Nicotiana tabacum A0A1S3ZYT7
-
-
1.1.1.284 Oryza sativa
-
-
-
1.1.1.284 Physcomitrium patens A0A2K1JM97
-
-
1.1.1.284 Pisum sativum P80572
-
-
1.1.1.284 Solanum lycopersicum D2Y3F4
-
-
1.1.1.284 Solanum tuberosum Q2XPW7
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.1.1.284 nitrosylation regulation of GSNOR activity through S-nitrosation of conserved cysteines is observed in Arabidopsis thaliana plants. Mono-, di-, and trinitrosation, which are confirmed by mass spectrometry, lead to subtle changes in enzyme conformation. GSNOR enzymatic activity, but not gene expression, is inhibited by the nitrogen assimilatory pathway via post-transcriptional S-nitrosation, preventing any scavenging of GSNO Arabidopsis thaliana

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.284 cell suspension culture
-
Arabidopsis thaliana
-
1.1.1.284 leaf
-
Solanum lycopersicum
-
1.1.1.284 leaf
-
Arabidopsis thaliana
-
1.1.1.284 leaf
-
Nicotiana tabacum
-
1.1.1.284 leaf
-
Cucumis sativus
-
1.1.1.284 leaf
-
Cucumis melo
-
1.1.1.284 leaf
-
Solanum tuberosum
-
1.1.1.284 leaf
-
Pisum sativum
-
1.1.1.284 root
-
Cucumis sativus
-
1.1.1.284 root
-
Cucumis melo
-
1.1.1.284 root
-
Pisum sativum
-
1.1.1.284 seedling
-
Helianthus annuus
-
1.1.1.284 stem
-
Cucumis sativus
-
1.1.1.284 stem
-
Cucumis melo
-
1.1.1.284 stem
-
Solanum tuberosum
-
1.1.1.284 stem
-
Pisum sativum
-
1.1.1.284 TBY-2 cell
-
Nicotiana tabacum
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.284 additional information in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO Oryza sativa ?
-
-
1.1.1.284 additional information in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO Solanum lycopersicum ?
-
-
1.1.1.284 additional information in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO Arabidopsis thaliana ?
-
-
1.1.1.284 additional information in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO Solanum tuberosum ?
-
-
1.1.1.284 additional information in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO Pisum sativum ?
-
-
1.1.1.284 additional information in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO Lotus japonicus ?
-
-
1.1.1.284 additional information in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a cosubstrate in the reduction of GSNO Chlamydomonas reinhardtii ?
-
-
1.1.1.284 additional information in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO Physcomitrium patens ?
-
-
1.1.1.284 additional information in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO Nicotiana tabacum ?
-
-
1.1.1.284 additional information in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO Helianthus annuus ?
-
-
1.1.1.284 additional information in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO Cucumis sativus ?
-
-
1.1.1.284 additional information in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO Cucumis melo ?
-
-
1.1.1.284 additional information in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO Nicotiana attenuata ?
-
-
1.1.1.284 additional information plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant Arabidopsis thaliana ?
-
-
1.1.1.284 additional information plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant Physcomitrium patens ?
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-
1.1.1.284 additional information plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant Nicotiana tabacum ?
-
-
1.1.1.284 additional information plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant Helianthus annuus ?
-
-
1.1.1.284 additional information plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant Cucumis sativus ?
-
-
1.1.1.284 additional information plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant Cucumis melo ?
-
-
1.1.1.284 additional information plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant Nicotiana attenuata ?
-
-
1.1.1.284 additional information plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant. GSNO is reduced with 15-20times higher catalytic efficiency compared to the oxidation of HMGSH Oryza sativa ?
-
-
1.1.1.284 additional information plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant. GSNO is reduced with 15-20times higher catalytic efficiency compared to the oxidation of HMGSH Solanum lycopersicum ?
-
-
1.1.1.284 additional information plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant. GSNO is reduced with 15-20times higher catalytic efficiency compared to the oxidation of HMGSH Solanum tuberosum ?
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1.1.1.284 additional information plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant. GSNO is reduced with 15-20times higher catalytic efficiency compared to the oxidation of HMGSH Pisum sativum ?
-
-
1.1.1.284 additional information plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant. GSNO is reduced with 15-20times higher catalytic efficiency compared to the oxidation of HMGSH Lotus japonicus ?
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1.1.1.284 S-(hydroxymethyl)glutathione + NAD+
-
Oryza sativa S-formylglutathione + NADH + H+
-
?
1.1.1.284 S-(hydroxymethyl)glutathione + NAD+
-
Solanum lycopersicum S-formylglutathione + NADH + H+
-
?
1.1.1.284 S-(hydroxymethyl)glutathione + NAD+
-
Arabidopsis thaliana S-formylglutathione + NADH + H+
-
?
1.1.1.284 S-(hydroxymethyl)glutathione + NAD+
-
Physcomitrium patens S-formylglutathione + NADH + H+
-
?
1.1.1.284 S-(hydroxymethyl)glutathione + NAD+
-
Nicotiana tabacum S-formylglutathione + NADH + H+
-
?
1.1.1.284 S-(hydroxymethyl)glutathione + NAD+
-
Helianthus annuus S-formylglutathione + NADH + H+
-
?
1.1.1.284 S-(hydroxymethyl)glutathione + NAD+
-
Cucumis sativus S-formylglutathione + NADH + H+
-
?
1.1.1.284 S-(hydroxymethyl)glutathione + NAD+
-
Cucumis melo S-formylglutathione + NADH + H+
-
?
1.1.1.284 S-(hydroxymethyl)glutathione + NAD+
-
Nicotiana attenuata S-formylglutathione + NADH + H+
-
?
1.1.1.284 S-(hydroxymethyl)glutathione + NAD+
-
Solanum tuberosum S-formylglutathione + NADH + H+
-
?
1.1.1.284 S-(hydroxymethyl)glutathione + NAD+
-
Pisum sativum S-formylglutathione + NADH + H+
-
?
1.1.1.284 S-(hydroxymethyl)glutathione + NAD+
-
Lotus japonicus S-formylglutathione + NADH + H+
-
?
1.1.1.284 S-(hydroxymethyl)glutathione + NAD+
-
Chlamydomonas reinhardtii S-formylglutathione + NADH + H+
-
?
1.1.1.284 S-nitrosoglutathione + NADH + H+
-
Oryza sativa GSSG + ammonia + NAD+
-
ir
1.1.1.284 S-nitrosoglutathione + NADH + H+
-
Solanum lycopersicum GSSG + ammonia + NAD+
-
ir
1.1.1.284 S-nitrosoglutathione + NADH + H+
-
Arabidopsis thaliana GSSG + ammonia + NAD+
-
ir
1.1.1.284 S-nitrosoglutathione + NADH + H+
-
Physcomitrium patens GSSG + ammonia + NAD+
-
ir
1.1.1.284 S-nitrosoglutathione + NADH + H+
-
Nicotiana tabacum GSSG + ammonia + NAD+
-
ir
1.1.1.284 S-nitrosoglutathione + NADH + H+
-
Helianthus annuus GSSG + ammonia + NAD+
-
ir
1.1.1.284 S-nitrosoglutathione + NADH + H+
-
Cucumis sativus GSSG + ammonia + NAD+
-
ir
1.1.1.284 S-nitrosoglutathione + NADH + H+
-
Cucumis melo GSSG + ammonia + NAD+
-
ir
1.1.1.284 S-nitrosoglutathione + NADH + H+
-
Nicotiana attenuata GSSG + ammonia + NAD+
-
ir
1.1.1.284 S-nitrosoglutathione + NADH + H+
-
Solanum tuberosum GSSG + ammonia + NAD+
-
ir
1.1.1.284 S-nitrosoglutathione + NADH + H+
-
Pisum sativum GSSG + ammonia + NAD+
-
ir
1.1.1.284 S-nitrosoglutathione + NADH + H+
-
Lotus japonicus GSSG + ammonia + NAD+
-
ir
1.1.1.284 S-nitrosoglutathione + NADH + H+
-
Chlamydomonas reinhardtii GSSG + ammonia + NAD+
-
ir

Subunits

EC Number Subunits Comment Organism
1.1.1.284 homodimer 2 * 40000, SDS-PAGE Solanum lycopersicum
1.1.1.284 More tomato GSNOR is a homodimeric enzyme consisting of two 40 kDa subunits containing a big catalytic and a small coenzyme-binding domain with an active site localized in a cleft between them. Non-catalytic domain includes a binding site for NAD+ coenzyme: six beta-strands of each coenzyme-binding domain form 12 pseudo-continuous beta-sheets. Each catalytic domain includes two zinc atoms. One of them is involved in the catalytic mechanism by activating the hydroxyl and carbonyl groups of substrates for transfer of hydride, and is bonded to Cys47, Cys177, His69, and either Glu70 or a water molecule. The second zinc atom is considered to have purely a structural role and is coordinated to four cysteine residues, Cys99, Cys102, Cys105, and Cys113 Solanum lycopersicum

Synonyms

EC Number Synonyms Comment Organism
1.1.1.284 ADH3
-
Oryza sativa
1.1.1.284 ADH3
-
Solanum lycopersicum
1.1.1.284 ADH3
-
Arabidopsis thaliana
1.1.1.284 ADH3
-
Physcomitrium patens
1.1.1.284 ADH3
-
Nicotiana tabacum
1.1.1.284 ADH3
-
Helianthus annuus
1.1.1.284 ADH3
-
Cucumis sativus
1.1.1.284 ADH3
-
Cucumis melo
1.1.1.284 ADH3
-
Nicotiana attenuata
1.1.1.284 ADH3
-
Solanum tuberosum
1.1.1.284 ADH3
-
Pisum sativum
1.1.1.284 ADH3
-
Lotus japonicus
1.1.1.284 ADH3
-
Chlamydomonas reinhardtii
1.1.1.284 alcohol dehydrogenase class-3 UniProt Arabidopsis thaliana
1.1.1.284 AtGSNOR
-
Arabidopsis thaliana
1.1.1.284 FALDH
-
Oryza sativa
1.1.1.284 FALDH
-
Solanum lycopersicum
1.1.1.284 FALDH
-
Arabidopsis thaliana
1.1.1.284 FALDH
-
Physcomitrium patens
1.1.1.284 FALDH
-
Nicotiana tabacum
1.1.1.284 FALDH
-
Helianthus annuus
1.1.1.284 FALDH
-
Cucumis sativus
1.1.1.284 FALDH
-
Cucumis melo
1.1.1.284 FALDH
-
Nicotiana attenuata
1.1.1.284 FALDH
-
Solanum tuberosum
1.1.1.284 FALDH
-
Pisum sativum
1.1.1.284 FALDH
-
Lotus japonicus
1.1.1.284 FALDH
-
Chlamydomonas reinhardtii
1.1.1.284 GSNOR
-
Oryza sativa
1.1.1.284 GSNOR
-
Solanum lycopersicum
1.1.1.284 GSNOR
-
Arabidopsis thaliana
1.1.1.284 GSNOR
-
Physcomitrium patens
1.1.1.284 GSNOR
-
Nicotiana tabacum
1.1.1.284 GSNOR
-
Helianthus annuus
1.1.1.284 GSNOR
-
Cucumis sativus
1.1.1.284 GSNOR
-
Cucumis melo
1.1.1.284 GSNOR
-
Nicotiana attenuata
1.1.1.284 GSNOR
-
Solanum tuberosum
1.1.1.284 GSNOR
-
Pisum sativum
1.1.1.284 GSNOR
-
Lotus japonicus
1.1.1.284 GSNOR
-
Chlamydomonas reinhardtii
1.1.1.284 HMGSH dehydrogenase
-
Oryza sativa
1.1.1.284 HMGSH dehydrogenase
-
Solanum lycopersicum
1.1.1.284 HMGSH dehydrogenase
-
Arabidopsis thaliana
1.1.1.284 HMGSH dehydrogenase
-
Physcomitrium patens
1.1.1.284 HMGSH dehydrogenase
-
Nicotiana tabacum
1.1.1.284 HMGSH dehydrogenase
-
Helianthus annuus
1.1.1.284 HMGSH dehydrogenase
-
Cucumis sativus
1.1.1.284 HMGSH dehydrogenase
-
Cucumis melo
1.1.1.284 HMGSH dehydrogenase
-
Nicotiana attenuata
1.1.1.284 HMGSH dehydrogenase
-
Solanum tuberosum
1.1.1.284 HMGSH dehydrogenase
-
Pisum sativum
1.1.1.284 HMGSH dehydrogenase
-
Lotus japonicus
1.1.1.284 HMGSH dehydrogenase
-
Chlamydomonas reinhardtii
1.1.1.284 PmGSNOR
-
Physcomitrium patens
1.1.1.284 S-nitrosoglutathione reductase
-
Oryza sativa
1.1.1.284 S-nitrosoglutathione reductase
-
Solanum lycopersicum
1.1.1.284 S-nitrosoglutathione reductase
-
Arabidopsis thaliana
1.1.1.284 S-nitrosoglutathione reductase
-
Physcomitrium patens
1.1.1.284 S-nitrosoglutathione reductase
-
Nicotiana tabacum
1.1.1.284 S-nitrosoglutathione reductase
-
Helianthus annuus
1.1.1.284 S-nitrosoglutathione reductase
-
Cucumis sativus
1.1.1.284 S-nitrosoglutathione reductase
-
Cucumis melo
1.1.1.284 S-nitrosoglutathione reductase
-
Nicotiana attenuata
1.1.1.284 S-nitrosoglutathione reductase
-
Solanum tuberosum
1.1.1.284 S-nitrosoglutathione reductase
-
Pisum sativum
1.1.1.284 S-nitrosoglutathione reductase
-
Lotus japonicus
1.1.1.284 S-nitrosoglutathione reductase
-
Chlamydomonas reinhardtii
1.1.1.284 SlGSNOR
-
Solanum lycopersicum

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.284 additional information GSNOR cannot use NADPH in the reduction of GSNO Oryza sativa
1.1.1.284 additional information GSNOR cannot use NADPH in the reduction of GSNO Solanum lycopersicum
1.1.1.284 additional information GSNOR cannot use NADPH in the reduction of GSNO Arabidopsis thaliana
1.1.1.284 additional information GSNOR cannot use NADPH in the reduction of GSNO Physcomitrium patens
1.1.1.284 additional information GSNOR cannot use NADPH in the reduction of GSNO Nicotiana tabacum
1.1.1.284 additional information GSNOR cannot use NADPH in the reduction of GSNO Helianthus annuus
1.1.1.284 additional information GSNOR cannot use NADPH in the reduction of GSNO Cucumis sativus
1.1.1.284 additional information GSNOR cannot use NADPH in the reduction of GSNO Cucumis melo
1.1.1.284 additional information GSNOR cannot use NADPH in the reduction of GSNO Nicotiana attenuata
1.1.1.284 additional information GSNOR cannot use NADPH in the reduction of GSNO Solanum tuberosum
1.1.1.284 additional information GSNOR cannot use NADPH in the reduction of GSNO Pisum sativum
1.1.1.284 additional information GSNOR cannot use NADPH in the reduction of GSNO Lotus japonicus
1.1.1.284 additional information GSNOR cannot use NADPH in the reduction of GSNO Chlamydomonas reinhardtii
1.1.1.284 NADH
-
Oryza sativa
1.1.1.284 NADH
-
Arabidopsis thaliana
1.1.1.284 NADH
-
Physcomitrium patens
1.1.1.284 NADH
-
Nicotiana tabacum
1.1.1.284 NADH
-
Helianthus annuus
1.1.1.284 NADH
-
Cucumis sativus
1.1.1.284 NADH
-
Cucumis melo
1.1.1.284 NADH
-
Nicotiana attenuata
1.1.1.284 NADH
-
Solanum tuberosum
1.1.1.284 NADH
-
Pisum sativum
1.1.1.284 NADH
-
Lotus japonicus
1.1.1.284 NADH
-
Chlamydomonas reinhardtii
1.1.1.284 NADH the coenzyme binding is associated with the catalytic zinc atoms movement towards Glu70 in the catalytic domain in a hydrogen-bonding interaction with the carboxylate oxygen of Glu70. In the SlGSNOR structure crystallized with NADH and GSH, the enzyme appears in closed conformation Solanum lycopersicum

Expression

EC Number Organism Comment Expression
1.1.1.284 Nicotiana tabacum both GSNOR mRNA and protein levels are decreased in tobacco plants after treatment with jasmonic acid, the hormone implicated in the wounding signal transduction down
1.1.1.284 Nicotiana attenuata both GSNOR mRNA and protein levels are decreased in tobacco plants after treatment with jasmonic acid, the hormone implicated in the wounding signal transduction down
1.1.1.284 Arabidopsis thaliana GSNOR gene expression is downregulated in Arabidopsis after wounding down
1.1.1.284 Helianthus annuus GSNOR is downregulated, at the level of gene and protein expression and enzymatic activity, in mechanically damaged sunflower (Helianthus annuus) seedlings, which in turn leads to an accumulation of S-nitrosothiols, specifically GSNO down
1.1.1.284 Pisum sativum in pea leaves treated with 0.05 mM cadmium, GSNOR expression and activity are decreased by about 30% down
1.1.1.284 Lotus japonicus water stress, a problem for plant growth and productivity, in Lotus japonicus leads to both oxidative and nitrosative stress. Among others, cellular NO and S-nitrosothiol content are increased, GSNOR activity is reduced, and protein tyrosine nitration is stimulated down
1.1.1.284 Chlamydomonas reinhardtii an important role of NO, GSNOR, and S-nitrosation in response to salt stress is described in Chlamydomonas reinhardtii. NO production via increased nitrate reductase, but not NOS-like enzyme, activity is induced by salt stress to trigger the defense response. Induction or inactivation of antioxidant enzymes and GSNOR varied in connection with the duration of salt stress. Short-term stress causes the enzymes to scavenge ROSs and RNSs and balance cellular redox status. Long-term stress inactivates them significantly by RNS-induced protein S-nitrosation, resulting in oxidative damage and reduced cell viability. Salt stress induced the accumulation of S-nitrosothiols and S-nitrosation of GSNOR, glutathione S-transferase, and ubiquitin-like protein; S-nitrosation is reduced by thioredoxin-h5 (TRXh5), while it is enhanced by GSNOR inhibitor DA additional information
1.1.1.284 Cucumis sativus enzyme expression levels at different light conditions in different tissues, overview additional information
1.1.1.284 Cucumis melo enzyme expression levels at different light conditions in different tissues, overview additional information
1.1.1.284 Pisum sativum enzyme expression levels at different light conditions in different tissues, overview additional information
1.1.1.284 Arabidopsis thaliana GSNOR enzymatic activity, but not gene expression, is inhibited by the nitrogen assimilatory pathway via post-transcriptional S-nitrosation, preventing any scavenging of GSNO. GSNOR activity is modulated in response to altered light conditions, as described for the first time in Arabidopsis thaliana HOT5 mutant plants grown in the dark additional information
1.1.1.284 Arabidopsis thaliana 40% increase in GSNOR activity is observed in plants grown in the presence of 0.5 mM arsenate, accompanied with a significant reduction of GSNO content and a significant increase in NO content up
1.1.1.284 Pisum sativum a significant increase in enzyme expression is observed in leaves of pea plants exposed to continuous light and continuous dark up
1.1.1.284 Cucumis sativus an increase in GSNOR activity in roots, stems, and leaves is observed in two genotypes of Cucumis spp., Curcumis sativus and Curcumis melo, exposed to mechanical damage of stem and leaf up
1.1.1.284 Cucumis melo an increase in GSNOR activity in roots, stems, and leaves is observed in two genotypes of Cucumis spp., Curcumis sativus and Curcumis melo, exposed to mechanical damage of stem and leaf up
1.1.1.284 Oryza sativa GSNOR gene expression and enzymatic activity are slightly higher and the enzymatic activity is significantly increased by NO treatment in rice plants grown under aluminum stress up
1.1.1.284 Solanum tuberosum in potato plants exposed to aluminum, GSNOR activity is not affected in roots and it is increased by about 20% and 45% in leaves and stems, respectively up

General Information

EC Number General Information Comment Organism
1.1.1.284 evolution GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1) Physcomitrium patens
1.1.1.284 evolution GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins Oryza sativa
1.1.1.284 evolution GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins Solanum lycopersicum
1.1.1.284 evolution GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins Arabidopsis thaliana
1.1.1.284 evolution GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins Nicotiana tabacum
1.1.1.284 evolution GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins Helianthus annuus
1.1.1.284 evolution GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins Cucumis sativus
1.1.1.284 evolution GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins Cucumis melo
1.1.1.284 evolution GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins Nicotiana attenuata
1.1.1.284 evolution GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins Solanum tuberosum
1.1.1.284 evolution GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins Pisum sativum
1.1.1.284 evolution GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins Lotus japonicus
1.1.1.284 evolution GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins Chlamydomonas reinhardtii
1.1.1.284 malfunction a fast increase in S-nitrosothiol content and a reduction of the leaf photosynthesis ratio are a result of suppressed GSNOR activity with specific inhibitors Oryza sativa
1.1.1.284 malfunction a fast increase in S-nitrosothiol content and a reduction of the leaf photosynthesis ratio are a result of suppressed GSNOR activity with specific inhibitors Solanum tuberosum
1.1.1.284 malfunction a fast increase in S-nitrosothiol content and a reduction of the leaf photosynthesis ratio are a result of suppressed GSNOR activity with specific inhibitors Pisum sativum
1.1.1.284 malfunction a potential role of GSNOR in plant resistance to herbivory Manduca sexta is examined in coyote tobacco (Nicotiana attenuata) plants using a virus-induced silencing of GSNOR. GSNOR-silenced plants are more susceptible to herbivore attack and decreased the herbivore-induced accumulation of phytohormones jasmonic acid (JA) and ethylene and activity of trypsin proteinase inhibitors Nicotiana attenuata
1.1.1.284 malfunction Arabidopsis thaliana plants overexpressing the GSNOR gene exhibit increased nitrate reductase (NR) activity, conversely, GSNOR mutant plants show a significant decrease in NR activity. GSNOR enzymatic activity, but not gene expression, is inhibited by the nitrogen assimilatory pathway via post-transcriptional S-nitrosation, preventing any scavenging of GSNO. Enzymatic activity of GSNOR is essential for the acclimation of Arabidopsis thaliana plants to high temperature, since HOT5 mutants, plants with defect GSNOR gene, are more sensitive to high temperature as a consequence of disturbed homeostasis of S-nitrosothiols and NO-derived ROS signaling pathways. Enzyme mutant Nox1 is an NO overproducing plant with higher levels of L-arginine and L-citrulline, while mutant Gsnor1-3 is a plant with reduced GSNOR activity with higher levels of NO, S-nitrosothiols, and nitrate. Gsnor1-3 mutant Arabidopsis thaliana plants with a high S-nitrosothiols level show an increased selenite tolerance. high NO level, due to the reduced GSNOR activity, increases sensitivity under mild stress conditions, while it supports tolerance under severe stress conditions. Gsnor1-3 mutant plants with a high S-nitrosothiols level show an increased selenite tolerance Arabidopsis thaliana
1.1.1.284 malfunction GSNOR overexpression in tomato plant has little effect on growth and development, whereas GSNOR downregulated plants are significantly smaller, suggesting a role for NO and S-nitrosothiol signaling Solanum lycopersicum
1.1.1.284 malfunction water stress, a problem for plant growth and productivity, in Lotus japonicus leads to both oxidative and nitrosative stress. Among others, cellular NO and S-nitrosothiol content are increased, GSNOR activity is reduced, and protein tyrosine nitration is stimulated Lotus japonicus
1.1.1.284 physiological function S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Important role of GSNOR and S-nitrosation in adaptation of Chlamydomonas reinhardtii to salt stress Chlamydomonas reinhardtii
1.1.1.284 physiological function S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR is involved in plant responses to cold and heat stress Solanum lycopersicum
1.1.1.284 physiological function S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR is involved in plant responses to cold and heat stress Physcomitrium patens
1.1.1.284 physiological function S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR is involved in plant responses to cold and heat stress Helianthus annuus
1.1.1.284 physiological function S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR is involved in plant responses to cold and heat stress Cucumis melo
1.1.1.284 physiological function S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. Regulation of GSNOR activity through S-nitrosation of conserved cysteines is observed in Arabidopsis thaliana plants. GSNOR activity might be regulated by high levels of NO donors. Changes in GSNOR levels have an influence on the activities of mitochondrial complex I, external NADH dehydrogenase, alternative oxidase and uncoupling protein. GSNOR modulates the activity of the mitochondrial respiratory chain through controlling NO/SNO homeostasis under physiological conditions and under nutritional stress. Regulatory mechanisms of GSNOR in protein denitrosation on the intersection of signaling pathways of ROSs and RNSs. GSNOR is involved in plant responses to cold and heat stress Arabidopsis thaliana
1.1.1.284 physiological function S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR is involved in plant responses to cold and heat stress. NO and GSNO, as S-nitrosating agents, and GSNOR are found to be involved in the programmed cell death (PCD) induced by heat shock or H2O2 in tobacco (Nicotiana tabacum) bright yellow-2 cells Nicotiana tabacum
1.1.1.284 physiological function S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR is involved in plant responses to cold and heat stress Cucumis sativus
1.1.1.284 physiological function S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR mediates some jasmonate-dependent responses, e.g., the accumulation of defense secondary metabolites. GSNOR is involved in plant responses to cold and heat stress Nicotiana attenuata
1.1.1.284 physiological function S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR modulates NO-induced nitrosative stress in rice plants grown under aluminum stress, which leads to accumulation of both ROSs and RNSs Oryza sativa
1.1.1.284 physiological function S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR modulates NO-induced nitrosative stress in rice plants grown under aluminum stress, which leads to accumulation of both ROSs and RNSs Solanum tuberosum
1.1.1.284 physiological function S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR modulates NO-induced nitrosative stress in rice plants grown under aluminum stress, which leads to accumulation of both ROSs and RNSs Pisum sativum
1.1.1.284 physiological function S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR modulates NO-induced nitrosative stress in rice plants grown under aluminum stress, which leads to accumulation of both ROSs and RNSs Lotus japonicus